Jump to content

Streptomycin 6-kinase

From Wikipedia, the free encyclopedia
streptomycin 6-kinase
Identifiers
EC no.2.7.1.72
CAS no.37278-11-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, a streptomycin 6-kinase (EC 2.7.1.72) is an enzyme that catalyzes the chemical reaction

ATP + streptomycin ADP + streptomycin 6-phosphate

Thus, the two substrates of this enzyme are ATP and streptomycin, whereas its two products are ADP and streptomycin 6-phosphate.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:streptomycin 6-phosphotransferase. Other names in common use include streptidine kinase, SM 6-kinase, streptomycin 6-kinase (phosphorylating), streptidine kinase (phosphorylating), streptomycin 6-O-phosphotransferase, and streptomycin 6-phosphotransferase. This enzyme participates in streptomycin biosynthesis.

References

[edit]
  • Walker JB, Skorvaga M (1973). "Phosphorylation of streptomycin and dihydrostreptomycin by Streptomyces. Enzymatic synthesis of different diphosphorylated derivatives". J. Biol. Chem. 248 (7): 2435–40. PMID 4121456.
  • Walker JB, Walker MS (1967). "Streptomycin biosynthesis. Enzymatic synthesis of O-phosphorylstreptidine from streptidine and adenosinetriphosphate". Biochim. Biophys. Acta. 148 (2): 335–41. doi:10.1016/0304-4165(67)90128-6. PMID 6075410.